Table I.
Description of MoRF Dataset
| Data set | MoRFs | Clusters | MoRFs per cluster |
|---|---|---|---|
| Initial MoRF dataset (5–25)a | 4289 | ||
| MoRF dataset with biological interaction (>400 Å2)b | 3837 | ||
| MoRF dataset with globular partner (>70)c | 3148 | ||
| MoRFs mapped to UniProt sequence databased | 1805 | ||
| MoRFs with overlapped region in mappinge | 1493 | 298 | 5.01 |
| MoRFs without 100% sequence identity in partners | 248 | 87 | 2.85 |
| MoRFs without 25% sequence identity in partners | 214 | 77 | 2.78 |
| MoRFs without atypical casesf | 61 | 23 | 2.65 |
MoRFs with 5–25 residues are the focus of this study.
400 Å2 cutoff was set to filter out the spurious interactions caused by crystal contacts.
Binding partners of MoRF are supposed to be globular proteins having more than 70 residues to fold into a certain conformation. The excluded ones includes interactions between short domain like SH3, chromo domain, A/B chain of insulin, Gramicidin-form ion channels, peptides forming amyloid-like fibril, alpha-helical coiled coil, and de novo proteins.
Most MoRFs cannot be mapped to UniProt are 5–9 residues in length.
MoRFs having one or more overlapping residues with each other.
Atypical cases include, for example, one MoRF bound to more than one partner in the same PDB entry and partners with subsequences that exactly match the entire sequence of another partner.